Structural prediction of sugar-binding proteins functional in chemotaxis and transport.
Comparisons of the D-galactose- and D-ribose-binding protein amino acid sequences and secondary structure predictions with the known primary and three-dimensional structure of L-arabinose-binding protein suggest that the three proteins have similar molecular structures. These studies also indicate an evolutionary relationship among the proteins. One region of striking homology between the galactose- and ribose-binding proteins suggests that this may be th protein-protein contact site for interaction with the membrane-bound chemotaxis receptor. The ligands and the geometry of the galactose binding site are also predicted.
D000595:Amino Acid Sequence; D001089:Arabinose / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism; D001692:Biological Transport; D002135:Calcium-Binding Proteins; D002352:Carrier Proteins / Q000378:metabolism; D002633:Chemotaxis; D004926:Escherichia coli / Q000378:metabolism; D029968:Escherichia coli Proteins; D005690:Galactose; D009004:Monosaccharide Transport Proteins; D033902:Periplasmic Binding Proteins; D011487:Protein Conformation; D012266:Ribose / Q000378:metabolism
C016242:AraF protein, E coli; D001426:Bacterial Proteins; D002135:Calcium-Binding Proteins; D002352:Carrier Proteins; D029968:Escherichia coli Proteins; D009004:Monosaccharide Transport Proteins; D033902:Periplasmic Binding Proteins; C028003:RbsB protein, E coli; C023550:galactose-binding protein; D012266:Ribose; D001089:Arabinose; D005690:Galactose